학술자료통계

Conference/Proceedings

Developement of novel enzyme system for production of enantiomerically pure β-amino$ acids : Kinetic resolution of racemic 3-amino-n-butanoic acid using transaminase from Alcaligenes denitrificans Y2k-2

(R,S)-3-amino-n-butanoic acid$(DL-\;{\beta}\;-homoalanine)$ has been kinetically resolved using Alcaligenes denitrificans Y2k-2 as a biocatalyst, which was isolated from soil by enrichment culture, which was carried out with minimal media containing (R,S)-3-amino-n-butanoic acid as a sole nitrogen source. The enzyme which peformed this kinetic resolution assumed to belong to the ${\omega}-transaminase$ family, because A. denitrificans used pyruvate as amino acceptor and its transaminase activity was inhibited by gabaculine, aminooxy acetic acid and hydroxylamine. In whole cell reaction, (R,S)-3-amino-n-butanoic acid was kinetically resolved to the corresponding (R)-3-amino-n-butanoic acid with excellent E (>100) in the presence of pyruvate as an amino acceptor at $37^{\circ}C$. (S-specific) We observed the substrate inhibition for pyruvate at 100mM. In this study, characteristics of transaminase activity of Alcaligenes denitrificans Y2k-2, such as substrate specificity and thermostability, are carried out for the development of (R)-3- amino-n-butanoic acid production system.

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